2.7.7.9: UTP-glucose-1-phosphate uridylyltransferase
This is an abbreviated version!
For detailed information about UTP-glucose-1-phosphate uridylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.9
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2.7.7.9
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phosphoglucomutase
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polysaccharide
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glycogen
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galactose
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udp-galactose
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adp-glucose
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exopolysaccharide
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dictyostelium
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udp-sugars
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udp-n-acetylglucosamine
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leloir
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galactose-1-phosphate
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udp-glucuronic
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galactokinase
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aureobasidium
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pyrophosphorolysis
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sucrose-phosphate
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gellan
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xylinum
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agriculture
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synthesis
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medicine
- 2.7.7.9
- phosphoglucomutase
- polysaccharide
- glycogen
- galactose
- udp-galactose
- adp-glucose
- exopolysaccharide
- dictyostelium
- udp-sugars
- udp-n-acetylglucosamine
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leloir
- galactose-1-phosphate
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udp-glucuronic
- galactokinase
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aureobasidium
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pyrophosphorolysis
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sucrose-phosphate
- gellan
- xylinum
- agriculture
- synthesis
- medicine
Reaction
Synonyms
All3274, CugP, cyanobacterial UDP-Glc PPase, ExoN, GalU, gfugp, Glc-1-P UTase, GlcNAc-1-P UTase, glucose 1-phosphate uridylyltransferase, glucose-1-phosphate urididyltransferase, glucose-1-phosphate uridyltransferase, glucose-1-phosphate uridylyltransferase, KF278717, plastid UDP-glucose pyrophosphorylase, rml-1, ScUGPase-1, sll1558, ST0452, ST0452 protein, STK_04520, sugar-1-P NTase, sugar-1-phosphate nucleotidylyltransferase, TaGalU, UDP glucose pyrophosphorylase, UDP-Glc pyrophosphorylase, UDP-GlcPPase, UDP-glucose pyrophosphorylase, UDP-glucose pyrophosphorylase 1, UDP-glucose pyrophosphorylase isoenzyme UGP5, UDP-glucose pyrophosphorylase UGP1, UDP-glucose pyrophosphorylase UGP2, UDP-glucose pyrophosphorylase UGP3, UDPG phosphorylase, UDPG pyrophosphorylase, UDPG-pyrophosphorylase, UDPglucose pyrophosphorylase, UDPGP, UGP, ugp-1, UGP1, UGP3, UgpA, UGPase, UGPase1, UGPase2, UGPG-PPase, UPD1, uridine 5'-diphosphoglucose pyrophosphorylase, uridine diphosphate-D-glucose pyrophosphorylase, uridine diphosphate-glucose pyrophosphorylase, uridine diphosphoglucose pyrophosphorylase, uridine-diphosphate glucose pyrophosphorylase, uridylyltransferase, glucose 1-phosphate, UTP/dTTP-glucose-1-phosphate uridylyl/thymidylyl transferase, UTP:alpha-D-glucose uridylyltransferase, UTP:glucose-1-phosphate uridylyltransferase, VldB
ECTree
2.7.7.9 UTP-glucose-1-phosphate uridylyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D130A
site-directed mutagenesis the mutant shows highly reduced activity compatred to the wild-type enzyme
R15A
site-directed mutagenesis the mutant shows highly reduced activity compatred to the wild-type enzyme
C123S
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site-directed mutagenesis, active enzyme, 7fold increase in Km for magnesium diphosphate, 2fold increased Ki for MgUTP2-, no longer sensitive to SH-reagents, e.g. iodoacetamide
E412D
site-directed mutagenesis, the mutation does not change the oligomeric state, the mutant shows 176% catalytic activity compared to the wild-type enzyme
E412K
site-directed mutagenesis, the mutant has a longer side chain with a reverse in charge showed obvious inhibitory effects which results in 78% reduced activity compared to the wild-type hUGPase activity
E412Q
site-directed mutagenesis, the mutation changes the charge property, but not the length of side chain and shows only a marginal increase in activity of 19% when compared with the wild-type protein
H266R
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site-directed mutagenesis, mutant enzyme is active and similar to the wild-type, 4fold decrease in Km and Ki for MgUTP
H446S
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site-directed mutagenesis, the mutant shows only slight dissociation and slightly reduced activity in forward and reverse reactionsactivity
H497A
I466T
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site-directed mutagenesis, the mutant shows dissociation of subunits, a tetramer appears in addition to di- and monomers, and highly reduced activity in forward and reverse reactions
I468K
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site-directed mutagenesis, the mutant shows dissociation of subunits, a tetramer appears in addition to di- and monomers, the mutant shows reduced activity in the reverse reaction
I487D
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site-directed mutagenesis, the mutant shows dissociation of subunits, and highly reduced activity in forward and reverse reactions
K4110S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
L492E
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site-directed mutagenesis, the mutant shows only slight dissociation and retains activity
N391P/L492E
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site-directed mutagenesis, inactive mutant showing dissociation into di- and monomers
N491P
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site-directed mutagenesis, the mutant shows reduced activity in the reverse reaction
N491P/L492E
site-directed mutagenesis, mutant N491P/L492E is constructed to depolymerize hUGPase octamers, the mutation in the C-terminal left-handed beta-helix changes the oligomerization state the mutant enzyme, that becomes monomeric, it shows about the double activity of the wild-type enzyme
P414G/T415P
site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state
R389H
-
site-directed mutagenesis, mutant enzyme is active and similar to the wild-type
R422Q
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site-directed mutagenesis, mutant enzyme is active and similar to the wild-type
R445H
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site-directed mutagenesis, mutant enzyme is active and similar to the wild-type
S309N/S311R
site-directed mutagenesis, mutation in sequence analogy to the Saccharomyces cerevisiae enzyme, the mutant shows 84% of wild-type activity
T406K/M407L
site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state
T448K
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site-directed mutagenesis, the mutant shows dissociation of subunits, a tetramer appears in addition to di- and monomers, and highly reduced activity in forward and reverse reactions
V416N
site-directed mutagenesis, the mutant shows activity similar to that of the wild-type hUGPase, the mutation does not change the oligomeric state
W218S
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site-directed mutagenesis, mutant enzyme is active and similar to the wild-type, increase in Km
C99S
site-directed mutagenesis, half Vmax of wild-type, 12fold higher Km for diphosphate, altered diphosphate binding
Ccut-101
101 amino acid residues deleted (exons 16-19, and 1 amino acid residue of exon 15)
Delta 1-4
deletion of 4 amino acid residues of the C-terminal domain, possibly involved in oligomerization
Delta 1-8
deletion of 8 amino acid residues of the C-terminal domain, possibly involved in oligomerization
Delta-NB
deletion mutant: amino acid residue 96-100 deleted (essential for catalysis)
D462H
natural mutation of isoform Ugp1, D462 in rice variety B5 is replaced by H462 in rice variety TN1
Y97A
Y97C
Y97D
Y97E
Y97F
Y97G
Y97H
Y97I
Y97K
Y97L
Y97M
Y97N
Y97Q
Y97R
Y97S
Y97T
Y97V
Y97W
A8G
mutant exhibits activity only for a combination of UTP and glucose 1-phosphate, similar to wild-type
additional information
H497A
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site-directed mutagenesis, the mutant shows dissociation of subunits, and highly reduced activity in forward and reverse reactions
H497A
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site-directed mutagenesis, the mutant shows only slight dissociation and retains full activity in the reverse eaction, but shows reduced reaction in the forward reaction
Y97A
specific Glc-1-P UTase activity of the mutant enzyme is 2.3fold lower than the specific activity of the mutant enzyme
Y97A
activity is 2.3fold lower than that of the wild-type enzyme
Y97A
the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97C
specific Glc-1-P UTase activity of the mutant enzyme is 1.9fold lower than the specific activity of the mutant enzyme
Y97C
activity is 1.87fold lower than that of the wild-type enzyme
Y97D
specific Glc-1-P UTase activity of the mutant enzyme is 6.2fold lower than the specific activity of the mutant enzyme
Y97D
activity is 6.2fold lower than that of the wild-type enzyme
Y97D
the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97F
specific Glc-1-P UTase activity of the mutant enzyme is 1.2fold lower than the specific activity of the mutant enzyme
Y97F
activity is 1.2fold lower than that of the wild-type enzyme
Y97F
the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97G
specific Glc-1-P UTase activity of the mutant enzyme is 4.2fold lower than the specific activity of the mutant enzyme
Y97G
activity is 4.2fold lower than that of the wild-type enzyme
Y97G
the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97H
specific Glc-1-P UTase activity of the mutant enzyme is 2.6fold higher than the specific activity of the mutant enzyme
Y97H
activity is 1.6fold lower than that of the wild-type enzyme
Y97H
the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97I
the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97K
specific Glc-1-P UTase activity of the mutant enzyme is 3.7fold lower than the specific activity of the mutant enzyme
Y97K
activity is 3.7fold lower than that of the wild-type enzyme
Y97K
the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97L
specific Glc-1-P UTase activity of the mutant enzyme is 2.4fold higher than the specific activity of the mutant enzyme
Y97L
activity is 2.4fold higher than that of the wild-type enzyme
Y97L
the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97M
specific Glc-1-P UTase activity of the mutant enzyme is 2.8fold higher than the specific activity of the mutant enzyme
Y97M
activity is 2.8fold higher than that of the wild-type enzyme
Y97M
the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97N
specific Glc-1-P UTase activity of the mutant enzyme is 4.1fold higher than the specific activity of the mutant enzyme
Y97N
activity is 4.1fold higher than that of the wild-type enzyme
Y97N
the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97Q
specific Glc-1-P UTase activity of the mutant enzyme is 1.04fold higher than the specific activity of the mutant enzyme
Y97Q
activity is 1.04fold higher than that of the wild-type enzyme
Y97Q
the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97S
specific Glc-1-P UTase activity of the mutant enzyme is 1.1fold higher than the specific activity of the mutant enzyme
Y97S
activity is 1.1fold higher than that of the wild-type enzyme
Y97S
the mutant shows increased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97T
specific Glc-1-P UTase activity of the mutant enzyme is 4fold lower than the specific activity of the mutant enzyme
Y97T
activity is 3.96fold lower than that of the wild-type enzyme
Y97T
the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
Y97V
specific Glc-1-P UTase activity of the mutant enzyme is 3.34fold lower than the specific activity of the mutant enzyme
Y97V
activity is 3.34fold lower than that of the wild-type enzyme
Y97V
the mutant shows decreased glucose-1-phosphate uridylyltransferase activity compared to the wild type enzyme
additional information
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enzyme gene disruption mutant reduces the survival of Aeromonas hydrophila in serum to less than 1%, decreases the ability of strains to adhere and reduces by 1.5 or 2 log units the virulence of Aeromonas serotype O34 strains in a septicaemia model. The mutant shows two types of lipopolysaccharide structures. The first one corresponds to a rough strain having the complete core, but lacking the terminal galactose residue from the LPS-core and 4-amino-4-deoxyarabinose residues from phosphate groups in lipid A. The second one corresponds to a deeply truncated structure with the LPS-core restricted to one 3-deoxy-D-manno-oct-2-ulosonic acid and three L-glycero-D-manno-heptose residues
additional information
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construction of transgenic plants, with increased or deleted expression of enzyme, study of sucrose effects on the enzyme and gene Ugp, respectively
additional information
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UGP2 is unable to replace UGP1 in UGP1 knockout lines
additional information
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UGP2 is unable to replace UGP1 in UGP1 knockout lines
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additional information
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truncation mutant DELTA 490-497 is almost inactive due to dissociation into di- and monomers
additional information
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overexpression of sucrose synthase and of UDP-glucose pyrophosphorylase. Single transgenic plants show significant increases in the height growth. Double-transgene plants demonstrate an additive effect and are even taller than single-transgene parents. Double-transgene plants may show increases in soluble sugar content. Both enzymes may be markers for sink strength
additional information
isoform Ugp1 silencing by RNAi results in male sterility of plants. Pollen mother cells of silenced plants appear normal before meiosis, but during meiosis, normal callose deposition is disrupted and the degeneration of the tapetum and middle layer is inhibited
additional information
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isoform Ugp1 silencing by RNAi results in male sterility of plants. Pollen mother cells of silenced plants appear normal before meiosis, but during meiosis, normal callose deposition is disrupted and the degeneration of the tapetum and middle layer is inhibited
additional information
generation of gain-of-function promoter-GUS fusion constructs, overview
additional information
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generation of gain-of-function promoter-GUS fusion constructs, overview
additional information
the UTP-glucose-1-phosphate uridylyltransferase activity of mutant enzyme DC005 is reduced by 10%, as compared to that of the wild-type ST0452 protein, while the activity of DC011 is increased by 18%, indicating that the enzymatic activity in the N-terminal region is not greatly affected by truncation of the C-terminal 5 or 11 residues. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80°C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C
